CHMU_TRIPA
ID CHMU_TRIPA Reviewed; 266 AA.
AC A0A0S0FTT9;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Chorismate mutase {ECO:0000303|PubMed:26579090};
DE Short=CM {ECO:0000305};
DE EC=5.4.99.5 {ECO:0000305|PubMed:26579090};
DE AltName: Full=TpARO7 {ECO:0000303|PubMed:26579090};
GN Name=ARO7 {ECO:0000303|PubMed:26579090};
GN ORFNames=A9Z42_0036180 {ECO:0000312|EMBL:OTA03187.1};
OS Trichoderma parareesei (Filamentous fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=858221;
RN [1] {ECO:0000312|EMBL:ALF39595.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=T6 {ECO:0000303|PubMed:26579090};
RX PubMed=26579090; DOI=10.3389/fmicb.2015.01181;
RA Perez E., Rubio M.B., Cardoza R.E., Gutierrez S., Bettiol W., Monte E.,
RA Hermosa R.;
RT "The importance of chorismate mutase in the biocontrol potential of
RT Trichoderma parareesei.";
RL Front. Microbiol. 6:1181-1181(2015).
RN [2] {ECO:0000312|Proteomes:UP000219286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 125925 {ECO:0000312|EMBL:OTA03187.1};
RX PubMed=26272569; DOI=10.1128/genomea.00885-15;
RA Yang D., Pomraning K., Kopchinskiy A., Karimi Aghcheh R., Atanasova L.,
RA Chenthamara K., Baker S.E., Zhang R., Shen Q., Freitag M., Kubicek C.P.,
RA Druzhinina I.S.;
RT "Genome Sequence and Annotation of Trichoderma parareesei, the Ancestor of
RT the Cellulase Producer Trichoderma reesei.";
RL Genome Announc. 3:e00885-e00885(2015).
CC -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC prephenate (PubMed:26579090). Acts at the first branch point in the
CC aromatic amino acid pathway where it steers biosynthesis towards
CC phenylalanine and tyrosine, and away from tryptophan (By similarity).
CC {ECO:0000250|UniProtKB:P32178, ECO:0000269|PubMed:26579090}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897,
CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5;
CC Evidence={ECO:0000305|PubMed:26579090};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13898;
CC Evidence={ECO:0000305|PubMed:26579090};
CC -!- ACTIVITY REGULATION: Each dimer has two allosteric binding sites that
CC can bind the regulatory effectors tryptophan or tyrosine (By
CC similarity). Can bind either one tryptophan or one tyrosine, two
CC tryptophan or two tyrosine or one tryptophan and one tyrosine, which
CC differentially affect the catalytic activity (By similarity). Activated
CC by tryptophan and subject to feedback inhibition by tyrosine (By
CC similarity). In the presence of both tryptophan and tyrosine, the
CC enzyme is in the activated state (By similarity).
CC {ECO:0000250|UniProtKB:P32178}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC prephenate from chorismate: step 1/1. {ECO:0000305|PubMed:26579090}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P32178}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32178}.
CC -!- INDUCTION: Induced by aromatic amino acids and chorismate.
CC {ECO:0000269|PubMed:26579090}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown decreases chorismate
CC mutase activity (PubMed:26579090). RNAi-mediated knockdown decreases
CC cell population growth rate (PubMed:26579090). RNAi-mediated knockdown
CC decreases antifungal activity against Fusarium oxysporum and Botrytis
CC cinerea (PubMed:26272569). {ECO:0000269|PubMed:26272569,
CC ECO:0000269|PubMed:26579090}.
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DR EMBL; KT240045; ALF39595.1; -; Genomic_DNA.
DR EMBL; LFMI01000387; OTA03187.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S0FTT9; -.
DR SMR; A0A0S0FTT9; -.
DR BRENDA; 5.4.99.5; 16178.
DR UniPathway; UPA00120; UER00203.
DR Proteomes; UP000219286; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; ISO:UniProtKB.
DR GO; GO:0004106; F:chorismate mutase activity; IMP:UniProtKB.
DR GO; GO:0046417; P:chorismate metabolic process; IMP:UniProtKB.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IC:UniProtKB.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IC:UniProtKB.
DR Gene3D; 1.10.590.10; -; 1.
DR InterPro; IPR036263; Chorismate_II_sf.
DR InterPro; IPR008238; Chorismate_mutase_AroQ_euk.
DR InterPro; IPR037039; CM_AroQ_sf_eucaryotic.
DR PANTHER; PTHR21145; PTHR21145; 1.
DR PIRSF; PIRSF017318; Chor_mut_AroQ_eu; 1.
DR SUPFAM; SSF48600; SSF48600; 1.
DR TIGRFAMs; TIGR01802; CM_pl-yst; 1.
DR PROSITE; PS51169; CHORISMATE_MUT_3; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Amino-acid biosynthesis;
KW Aromatic amino acid biosynthesis; Cytoplasm; Isomerase;
KW Phenylalanine biosynthesis; Tyrosine biosynthesis.
FT CHAIN 1..266
FT /note="Chorismate mutase"
FT /id="PRO_0000452014"
FT DOMAIN 7..263
FT /note="Chorismate mutase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00516"
FT BINDING 77
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 78
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 144
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 144
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 146
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 146
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 147
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 147
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 150
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
SQ SEQUENCE 266 AA; 30982 MW; EF9D0885AA43804B CRC64;
MDSAVDMADS ERALNLTHIR FQLIRLEDTI TFHLIERVQF PYNKTIYTPG AISIPDSKLS
FFDWYFFQQE KLQSLIRRFE SPDEYPYFPE AVQKPILKPL NYPKILHNNT VCVNDKIKKF
YIEKFLPKVC PDFGREDRGE AQENYGSTST CDIACLQALS RRIHFGKFVA ESKFQSDPEY
YTKLIQAEDR EAIGESITNA AVEKQVLDRL RLKVETYGKD PSLLEGVEQP IKINVDAVVS
MYKDFVIPLT KEVEVEYLMQ RLIPEE
